Structure and Non-Structure of Centrosomal Proteins
Open accessAbstract
Here we perform a large-scale study of the structural properties and the expression of proteins that constitute the human Centrosome. Centrosomal proteins tend to be larger than generic human proteins (control set), since their genes contain in average more exons (20.3 versus 14.6). They are rich in predicted disordered regions, which cover 57% of their length, compared to 39% in the general human proteome. They also contain several regions that are dually predicted to be disordered and coiled-coil at the same time: 55 proteins (15%) contain disordered and coiled-coil fragments that cover more than 20% of their length. Helices prevail over strands in regions homologous to known structures (47% predicted helical residues against 17% predicted as strands), and even more in the whole centrosomal proteome (52% against 7%), while for control human proteins 34.5% of the residues are predicted as helical and 12.8% are predicted as strands. This difference is mainly due to residues predicted as disordered and helical (30% in centrosomal and 9.4% in control proteins), which may correspond to alpha-helix forming molecular recognition features (α-MoRFs). We performed expression assays for 120 full-length centrosomal proteins and 72 domain constructs that we have predicted to be globular. These full-length proteins are often insoluble: Only 39 out of 120 expressed proteins (32%) and 19 out of 72 domains (26%) were soluble. We built or retrieved structural models for 277 out of 361 human proteins whose centrosomal localization has been experimentally verified. We could not find any suitable structural template with more than 20% sequence identity for 84 centrosomal proteins (23%), for which around 74% of the residues are predicted to be disordered or coiled-coils. The three-dimensional models that we built are available at http://ub.cbm.uam.es/centrosome/models/index.php.
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Human centrosomal proteins are significantly biased toward being unstructured and having coiled-coil regions compared with generic human proteins.
“Bioinformatics analysis indicated that human centrosomal proteins have a significant bias to be both unstructured and with coiled-coil regions with respect to generic human proteins.”
From Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell (2016) · cites this paper as [526]
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- Authors
- Dos Santos, H. G., Abia, D., Janowski, R., Mortuza, G., Bertero, M. G., Boutin, M., Guarín, N., Méndez-Giraldez, R., Nuñez, A., Pedrero, J. G., Redondo, P., Sanz, M., Speroni, S., Teichert, F., Bruix, M., Carazo, J. M., Gonzalez, C., Reina, J., Valpuesta, J. M., Vernos, I., Zabala, J. C., Montoya, G., Coll, M., Bastolla, U., & Serrano, L.
- Affiliations
- Consejo Superior de Investigaciones Científicas (ES)
- Institute for Research in Biomedicine (ES)
- Spanish National Cancer Research Centre (ES)
- Centre for Genomic Regulation (ES)
- Institució Catalana de Recerca i Estudis Avançats (ES)
- Universidad de Cantabria (ES)
- Corresponding author
- Bastolla, Ugo
- Serrano, Luis
- ORCID
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-05-09
- Volume
- 8
- Issue
- 5
- Pages
- e62633
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3650010
- OpenAlex
- W2089316140
- Cited by
- 31
- References
- 58
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 3 · 2023: 1 · 2022: 3 · 2021: 1 · 2020: 3 · 2019: 2 · 2017: 2 · 2016: 4 · 2015: 2 · 2014: 5 · 2013: 1
- FWCI
- 1.79
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (publishedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Repositori digital de la UPF (Universitat Pompeu Fabra) (submittedVersion, cc-by)
- UCrea (University of Cantabria) (submittedVersion, cc-by)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- centrosome, centrosomal proteins, intrinsically disordered regions, coiled-coil domain, protein structure prediction, protein solubility, protein expression, exon number, alpha-helix content, structural model
- MeSH terms
- Amino Acid Sequence, Humans, Molecular Sequence Data, Protein Binding, Proteins, Signal Transduction, Gene Expression, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Folding, Centrosome, Protein Isoforms, Proteome, Databases, Protein
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